Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

被引：230

作者：

Kurouski, Dmitry ^{[1
]}

Van Duyne, Richard P. ^{[1
]}

Lednev, Igor K. ^{[2
]}

机构：

[1] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

[2] SUNY Albany, Dept Chem, Albany, NY 12222 USA

来源：

ANALYST | 2015年 / 140卷 / 15期

基金：

美国国家科学基金会;

关键词：

ULTRAVIOLET RESONANCE RAMAN; VIBRATIONAL CIRCULAR-DICHROISM; AMIDE-III VIBRATION; LYSOZYME FIBRILLATION; SUPRAMOLECULAR CHIRALITY; SINGLE; PEPTIDE; RESOLUTION; DENATURATION; NANOSCALE;

D O I：

10.1039/c5an00342c

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Amyloid fibrils are beta-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

引用

页码：4967 / 4980

页数：14

共 108 条

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